Recent protein crystallographic results show that beta pleated sheets are quite prevalent in globular proteins and enzymes. Nevertheless, model studies of the beta structure are scanty, largely because of the general intractability of this conformation. In order to enhance our understanding of the conformational attributes of the beta structure it is our objective to elaborate a comprehensive description of its equilibrium and dynamic characteristics in synthetic polypeptides and in proteins. Recent studies by us have identified conditions under which a soluble monomolecular beta form occurs in aqueous solution for two different polypeptide systems. It is intended to seek out nonaggregated beta structures in other systems as well. A combination of thermodynamic and hydrodynamic investigations on these systems will provide quantitative information on the stability and molecular shapes of these structures. The potentials of each amino acid for forming beta structures and beta turns are also susceptible of evaluation in this project. Kinetic studies of disordered-beta transitions will lead to the formulation of appropriate dynamic models for the generation of the beta structure, with the special intent of understanding the role of beta nucleation. Analogous experiments are to be carried out on globular proteins endowed with large proportions of the beta conformation. Our studies should yield a deeper appreciation of principles of protein structural chemistry and function and of the mechanism of protein folding.